Carbohydrate Structure and Cell Differentitation: Unique Properties of Fucosyl-glycopeptides Isolated from Embryonal Carcinoma Cells

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1978 May 1

PMID 276874

Citations 22

Authors

T Muramatsu

G Gachelin

J F Nicolas

H Condamine

H Jakob

F Jacob

Affiliations

Soon will be listed here.

Abstract

From embryonal carcinoma cells labeled with fucose, two main classes of glycopeptide products of Pronase digestion can be distinguished by Sephadex G-50 column chromatography: one eluted near the excluded volume and a smaller one. The large fucosyl-glycopeptides are scarcely present in differentiated cells derived from embryonal carcinoma cells (i.e., fibroblastlike cells, myoblasts, and parietal yolk-sac carcinoma). During in vitro differentiation of embryonal carcinoma cells, these large glycopeptides disappear almost completely. The small glycopeptides were analyzed by paper electrophoresis, concanavalin A-Sepharose affinity chromatography, and digestion with an endoglycosidase. The major components of these glycopeptides from embryonal carcinoma cells appear to be different from complex glycopeptides known to occur in adult cells. The glycopeptide pattern of mouse preimplantation embryos resembles that of embryonal carcinoma cells. These results suggest that the carbohydrate profile changes fundamentally during early stages of mammalian development.

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